ID   MFNB_METTH              Reviewed;         236 AA.
AC   O26244;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=(5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681};
DE            EC=4.2.3.153 {ECO:0000255|HAMAP-Rule:MF_00681};
DE   AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681};
DE            Short=4-HFC-P synthase {ECO:0000255|HAMAP-Rule:MF_00681};
GN   Name=mfnB {ECO:0000255|HAMAP-Rule:MF_00681}; OrderedLocusNames=MTH_141;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Catalyzes the formation of 4-(hydroxymethyl)-2-
CC       furancarboxaldehyde phosphate (4-HFC-P) from two molecules of
CC       glyceraldehyde-3-P (GA-3-P). {ECO:0000255|HAMAP-Rule:MF_00681}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-
CC         furancarboxaldehyde phosphate + 2 H2O + phosphate;
CC         Xref=Rhea:RHEA:43536, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:83407; EC=4.2.3.153;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00681};
CC   -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00681}.
CC   -!- SIMILARITY: Belongs to the MfnB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00681}.
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DR   EMBL; AE000666; AAB84647.1; -; Genomic_DNA.
DR   PIR; G69054; G69054.
DR   RefSeq; WP_010875780.1; NC_000916.1.
DR   AlphaFoldDB; O26244; -.
DR   SMR; O26244; -.
DR   STRING; 187420.MTH_141; -.
DR   EnsemblBacteria; AAB84647; AAB84647; MTH_141.
DR   GeneID; 1470102; -.
DR   KEGG; mth:MTH_141; -.
DR   PATRIC; fig|187420.15.peg.114; -.
DR   HOGENOM; CLU_068659_0_0_2; -.
DR   OMA; NFPWVIR; -.
DR   UniPathway; UPA00080; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:2001120; P:methanofuran biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00681; MfnB; 1.
DR   InterPro; IPR007565; 4HFCP_synth.
DR   InterPro; IPR035081; 4HFCP_synth_arc.
DR   Pfam; PF04476; 4HFCP_synth; 1.
DR   PIRSF; PIRSF015957; UCP015957; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..236
FT                   /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT                   /id="PRO_0000134868"
FT   ACT_SITE        27
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
FT   ACT_SITE        85
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
SQ   SEQUENCE   236 AA;  25092 MW;  0FF4D09AB56A4B1E CRC64;
     MLLLISPINT EEALEAIEGG ADIVDVKNPA EGSLGANFPW VIRRVREMTP EDMLVSATLG
     DVPYKPGTVS LAAMGALVSG ADYIKVGLYG TRNYDEAVDV MKNVVRAVKD QSDAIVVAAG
     YADAHRVGAV EPMEIPRVAA DSGADLAMLD TAVKDGKTLF DFMDMEKLES FVSAARDHGL
     KSALAGSVGR EHLKPLHEIG CDVVGIRGAA CVGGDRNTGR IHRDAVRELK ELLDSF